Open AccessStructure d'un glycoside de peptidolipide isolé d'une mycobactérie
Author(s) -
Laneelle G.,
Asselineau J.
Publication year - 1968
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1968.tb00396.x
Subject(s) - chemistry , edman degradation , glycopeptide , phenylalanine , peptide bond , threonine , glycosidic bond , stereochemistry , hydrolysis , amino acid , acid hydrolysis , peptide , alanine , amide , derivative (finance) , glycoside , peptide sequence , organic chemistry , biochemistry , enzyme , serine , economics , financial economics , gene , antibiotics
We isolated a mixture of glyco‐peptidolipids (mycosides C) from a non‐photochromogenic atypical strain of Mycobacteria. The main component, mycoside C 1217 , contains a 3 D‐hydroxyacid with 28 carbons, two 6‐deoxysugars and four amino compounds. The two sugars are 6‐deoxytalose and trimethylrhamnose (a minor component contains 3,4‐dimethylrhamnose instead of trimethylrhamnose). The four amino compounds are three aminoacids, phenylalanine, allo threonine and alanine, plus an aminoalcool identified with alaninol by gas chromatography of the N ‐trifluoracetyl derivative. The phenylalanine is N‐terminal in the peptide, and linked to the fatty acid by an amide bond. We established, by β‐elimination in alkaline medium, that the deoxytalose is linked to the hydroxyl of the allo ‐threonine by a glycosidic bond. After a mild hydrolysis of the mycoside, we isolated a glycopeptide containing allo ‐threonine, alanine, alaninol and trimethylrhamnose. By use of the dimethylamino‐naphtalene sulfonyl method end of Edman degradation, we have shown that the sequences of this glycopeptide is: allo ‐threonyl‐alanyl‐alaninol‐trimethylrhamnose All these results, along with those obtained from some other reactions, support the following structure for the mycoside C 1217 , which is in agreement with mass spectrometric results: